Activation of GCN2 kinase by ribosome stalling links translation elongation with translation initiation

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

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Moderated estimation of fold change and dispersion for RNA-seq data with DESeq2

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Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources

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A Direct Approach to False Discovery Rates

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XBP1 mRNA Is Induced by ATF6 and Spliced by IRE1 in Response to ER Stress to Produce a Highly Active Transcription Factor

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Mutation of the mouse klotho gene leads to a syndrome resembling ageing

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An Integrated Stress Response Regulates Amino Acid Metabolism and Resistance to Oxidative Stress

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FMRP Stalls Ribosomal Translocation on mRNAs Linked to Synaptic Function and Autism

Darnell, J. C., Van Driesche, S. J., Zhang, C., Hung, K. Y. S., Mele, A., Fraser, C. E., Stone, E. F., Chen, C., Fak, J. J., Chi, S. W., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.013 · Cited by 2,072

Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells

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ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death

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Limiting glutamine utilization activates a GCN2/TRAIL-R2/Caspase-8 apoptotic pathway in glutamine-addicted tumor cells

Yerbes, R., Mora-Molina, R., Fernández-Farrán, F. J., Hiraldo, L., López‐Rivas, A., & Palacios, C. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05346-y · Cited by 19

A mitochondrial long-chain fatty acid oxidation defect leads to transfer RNA uncharging and activation of the integrated stress response in the mouse heart

Ranea‐Robles, P., Pavlova, N. N., Bender, A. S., Pereyra, A. S., Ellis, J. M., Stauffer, B. B., Yu, C., Thompson, C. B., Argmann, C., Puchowicz, M. A., et al. (2022) · Cardiovascular Research · doi:10.1093/cvr/cvac050 · Cited by 18

The coupling of translational control and stress responses

Houston, R., Sekine, S., & Sekine, Y. (2020) · The Journal of Biochemistry · doi:10.1093/jb/mvaa061 · Cited by 17

Ribosome association inhibits stress-induced gene mRNA localization to stress granulesPreprint

Helton, N. S., Dodd, B. J. T., & Moon, S. L. (2025) · Genes & Development · doi:10.1101/gad.352899.125 · Cited by 22

Astragalus polysaccharide alleviates oxidative stress and senescence in chondrocytes in osteoarthritis via GCN2/ATF4/TXN axis

Chen, K., Qin, C., Ji, C.-Y., Yu, Y., Wu, Y., Xu, L., Jiang, Y., & Zou, G. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143285 · Cited by 20

A cell-based chemical-genetic screen for amino acid stress response inhibitors reveals torins reverse stress kinase GCN2 signaling

Brüggenthies, J. B., Fiore, A., Russier, M., Bitsina, C., Brötzmann, J., Kordes, S., Menninger, S., Wolf, A., Conti, E., Eickhoff, J., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102629 · Cited by 15

Emerging Role of GCN1 in Disease and Homeostasis

Tatara, Y., Kasai, S., Kokubu, D., Tsujita, T., Mimura, J., & Itoh, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052998 · Cited by 16

Regulatory Mechanisms of Aging Through the Nutritional and Metabolic Control of Amino Acid Signaling in Model Organisms

Obata, F., & Miura, M. (2024) · Annual Review of Genetics · doi:10.1146/annurev-genet-111523-102042 · Cited by 18

Novel insights into the GCN2 pathway and its targeting. Therapeutic value in cancer and lessons from lung fibrosis development

Piecyk, M., Ferraro‐Peyret, C., Laville, D., Perros, F., & Chaveroux, C. (2024) · FEBS Journal · doi:10.1111/febs.17203 · Cited by 19

eEF2K regulates pain through translational control of BDNF

Smith, P. R., Garcia, G., Meyer, A. R., Ryazanov, A. G., Ma, T., Loerch, S., & Campbell, Z. T. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.11.023 · Cited by 17

mTORC1 senses glutamine and other amino acids through GCN2

Figlia, G., Müller, S., Cortizo, F. G., Neff, M., Klinke, G., Poschet, G., & Teleman, A. A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00505-1 · Cited by 16

Run, Ribosome, Run: From Compromised Translation to Human Health

Vind, A., Snieckute, G., Bekker‐Jensen, S., & Blasius, M. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2022.0157 · Cited by 17

The molecular aetiology of tRNA synthetase depletion: induction of a GCN4 amino acid starvation response despite homeostatic maintenance of charged tRNA levels

McFarland, M. R., Keller, C. D., Childers, B. M., Adeniyi, S. A., Corrigall, H., Raguin, A., Romano, M. C., & Stansfield, I. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa055 · Cited by 14

The integrated stress response in the brain: cell type-specific functions in health and neurological disorders

Ho-Tieng, D., Sharma, V. K., Sonenberg, N., Gkogkas, C. G., & Khoutorsky, A. (2025) · Trends in Neurosciences · doi:10.1016/j.tins.2025.08.002 · Cited by 14

Ciclopirox Inhibition of eIF5A Hypusination Attenuates Fibroblast Activation and Cardiac Fibrosis

Subbaiah, K. C. V., Wu, J., Tang, W. H. W., & Yao, P. (2023) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd10020052 · Cited by 14

Gcn2 structurally mimics and functionally repurposes the HisRS enzyme for the integrated stress response

Bou‐Nader, C., Gaikwad, S., Bahmanjah, S., Zhang, F., Hinnebusch, A. G., & Zhang, J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2409628121 · Cited by 14

Insights into the role of collided ribosomes during the activation of the integrated stress response

Urs, A. N. N., Kim, L., & Zaher, H. S. (2025) · Biochemical Society Transactions · doi:10.1042/bst20253034 · Cited by 15

AMPKα2 signals amino acid insufficiency to inhibit protein synthesis

Mao, Y.-Z., Cui, M., Jiang, Y., Yu, H., Wang, M., Li, G., Zhang, H., Zhao, C., Shen, Y., An, Y., et al. (2025) · Cell Metabolism · doi:10.1016/j.cmet.2025.09.004 · Cited by 13

Stress and Liver Fibrogenesis

Hanquier, Z., Misra, J., Baxter, R., & Maiers, J. L. (2023) · American Journal Of Pathology · doi:10.1016/j.ajpath.2023.06.006 · Cited by 15

The amino acid sensor GCN2 suppresses terminal oligopyrimidine (TOP) mRNA translation via La-related protein 1 (LARP1)

Farooq, Z., Kusuma, F., Burke, P., Dufour, C. R., Lee, D., Tabatabaei, N., Toboz, P., Radovani, E., Greenblatt, J., Rehman, J., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102277 · Cited by 14

Translation from the Ribosome to the Clinic: Implication in Neurological Disorders and New Perspectives from Recent Advances

Hui, K. K., Chen, Y., Endo, R., & Tanaka, M. (2019) · Biomolecules · doi:10.3390/biom9110680 · Cited by 12

Signaling plasticity in the integrated stress response

Boone, M., & Zappa, F. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1271141 · Cited by 14

Multifaceted control of mRNA translation machinery in cancer

Alboushi, L., Hackett, A. P., Naeli, P., Bakhti, M., & Jafarnejad, S. M. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.110037 · Cited by 13

Ribosome changes reprogram translation for chemosurvival in G0 leukemic cells

Datta, C., Truesdell, S. S., Wu, K. Q., Bukhari, S. I. A., Ngue, H., Buchanan, B., Tonquèze, O. L., Lee, S., Kollu, S., Granovetter, M. A., et al. (2022) · Science Advances · doi:10.1126/sciadv.abo1304 · Cited by 15

Lost in translation: How neurons cope with tRNA decoding

Guo, W., Russo, S., & Tuorto, F. (2024) · BioEssays · doi:10.1002/bies.202400107 · Cited by 11

Murine Norovirus Infection Results in Anti-inflammatory Response Downstream of Amino Acid Depletion in Macrophages

Brocard, M., Lu, J. Q., Hall, B. S., Borah, K., Möller‐Levet, C. S., Georgana, I., Sorgeloos, F., Beste, D. J. V., Goodfellow, I., & Locker, N. (2021) · Journal of Virology · doi:10.1128/jvi.01134-21 · Cited by 11

An Overview of Methods for Detecting eIF2α Phosphorylation and the Integrated Stress Response

Krzyżosiak, A., Pitera, A. P., & Bertolotti, A. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1975-9_1 · Cited by 14

From the integrated stress response to oxidative stress: A historical perspective

Amiri, M., Toboz, P., Bellucci, M. A., Tahmasebi, S., & Sonenberg, N. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110958 · Cited by 11

Quality control and signaling pathways at stalled ribosomes

Chang, W. D., & Choe, Y. (2026) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01623-w · Cited by 17

Halofuginone triggers a transcriptional program centered on ribosome biogenesis and function in honey bees

Flores, M. E., McNamara-Bordewick, N. K., Lovinger, N. L., & Snow, J. W. (2021) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2021.103667 · Cited by 10

Structural Impact of 3-methylcytosine Modification on the Anticodon Stem-loop of a Neuronally-enriched Arginine tRNA

Berger, K. D., Puthenpeedikakkal, A. M. K., Mathews, D. H., & Fu, D. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169096 · Cited by 9

Contributions of Ccr4 and Gcn2 to the Translational Response of C. neoformans to Host-Relevant Stressors and Integrated Stress Response Induction

Knowles, C. M., Goich, D., Bloom, A. L., Kalem, M. C., & Panepinto, J. (2022) · bioRxiv · doi:10.1128/mbio.00196-23 · Cited by 6

RNA Damage Responses in Cellular Homeostasis, Genome Stability, and Disease

Zaher, H. S., & Mosammaparast, N. (2024) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-111523-023516 · Cited by 8

IGHMBP2 deletion suppresses translation and activates the integrated stress response

Park, J. E., Desai, H., Liboy-Lugo, J., Gu, S., Jowhar, Z. M., Xu, A., & Floor, S. N. (2024) · Life Science Alliance · doi:10.26508/lsa.202302554 · Cited by 7

Tools for Assessing Translation in Cryptococcus neoformans

Knowles, C. M., McIntyre, K. M., & Panepinto, J. C. (2021) · Journal of Fungi · doi:10.3390/jof7030159 · Cited by 9

Phosphoglycerate dehydrogenase is required for kernel development and defines a predominant serine synthesis pathway in maize

Zhang, Y., Li, R., Zheng, D., Zhao, J., Qing, K., He, R., Ma, Z., Chen, J., Xue, N., Tian, X., et al. (2025) · The Plant Cell · doi:10.1093/plcell/koaf126 · Cited by 8

The Integrated Stress Response in Cancer: Paradox and Therapeutic Promise

Zhang, C., Zhang, T., Tang, Q., Zeng, Y., & Cao, D. (2026) · Comprehensive physiology · doi:10.1002/cph4.70105 · Cited by 7

Is there a localized role for translational quality control?

Meydan, S., & Guydosh, N. R. (2023) · RNA · doi:10.1261/rna.079683.123 · Cited by 7

Interplay between stress-related genes may influence Alzheimer’s disease development: The results of genetic interaction analyses of human data

Yashin, A. I., Wu, D., Arbeev, K. G., Bagley, O., Akushevich, I. V., Duan, M., Yashkin, A. P., & Ukraintseva, S. V. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111477 · Cited by 7

Molecular basis of neurodegeneration in a mouse model of Polr3-related disease

Moir, R. D., Merheb, E., Chiţu, V., Stanley, E. R., & Willis, I. M. (2024) · eLife · doi:10.7554/elife.95314.3 · Cited by 7

Functional dissection of Alzheimer’s disease brain gene expression signatures in humans and mouse modelsPreprint

Wan, Y., Al-Ouran, R., Mangleburg, C. G., Lee, T. V., Allison, K., Neuner, S., Kaczorowski, C. C., Phillip, V., Howell, G. R., Martini-Stoica, H., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/506873 · Cited by 5

Detecting ribosome collisions with differential rRNA fragment analysis in ribosome profiling data

Kyei-Baffour, E. S., Bak, J., Silva, J., Faller, W. J., & Alkan, F. (2025) · NAR Genomics and Bioinformatics · doi:10.1093/nargab/lqaf045 · Cited by 5

GCN2 monitors mRNA translation termination

Worner, K., Maschhoff, K. R., Schuh, G. M., & Hu, W. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.11.015 · Cited by 6

Aberrant mitochondrial aggregation of TDP-43 activated mitochondrial unfolded protein response and contributed to recovery of acetaminophen induced acute liver injury

Liu, Z., Qiang, Y., Shan, S., Wang, S., Liu, Z. Q., Yang, Y., Huang, Z., Song, M., Zhao, X., & Song, F. (2024) · Toxicology Research · doi:10.1093/toxres/tfae008 · Cited by 6

The Relationship Between Ribosome-Associated Quality Control and Neurological Disorders

Wang, J., Wang, J., Cao, H., Xing, Y., Wang, Z., Ma, J., Zhao, R., Zhang, W., Guo, J., & Chang, X. (2024) · The Journals of Gerontology Series A · doi:10.1093/gerona/glae304 · Cited by 5

An ISR-independent role of GCN2 prevents excessive ribosome biogenesis and mRNA translation

Román-Trufero, M., Kleijn, I. T., Blighe, K., Zhou, J., Saavedra-García, P., Gaffar, A., Christoforou, M., Bellotti, A., Abrahams, J. M., Atrih, A., et al. (2025) · Life Science Alliance · doi:10.26508/lsa.202403014 · Cited by 9

Serine mistranslation induces the integrated stress response through the P stalk

Zhang, H., & Ling, J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108447 · Cited by 6

Alternating hemiplegia of childhood associated mutations in Atp1a3 reveal diverse neurological alterations in mice

Terrey, M., Krivoshein, G., Adamson, S. I., Arystarkhova, E., Anderson, L. C., Szwec, J., McKee, S., Jones, H., Perkins, S., Selvam, V., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106954 · Cited by 5

Translation elongation: measurements and applications

Watkins, L., Li, M., & Wu, B. (2025) · RNA Biology · doi:10.1080/15476286.2025.2504727 · Cited by 7

PEPseq quantifies transcriptome-wide changes in protein occupancy and reveals selective translational repression after translational stress

Trendel, J., Boileau, E., Jochem, M., Dieterich, C., & Krijgsveld, J. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad557 · Cited by 6

Early steps in the biogenesis of mitochondrially encoded oxidative phosphorylation subunits

Jung, S., Sridhara, S., & Ott, M. (2023) · IUBMB Life · doi:10.1002/iub.2784 · Cited by 5

Stressing out translation

Mellado, W., & Willis, D. E. (2021) · Science · doi:10.1126/science.abk3261 · Cited by 6

Regulation of translation elongation and integrated stress response in heat-shocked neurons

Seluzicki, C. M., Razavi-Mohseni, M., Türker, F., Patel, P., Hua, B., Beer, M., Goff, L. A., & Margolis, S. S. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115639 · Cited by 5

Comparative CRISPRi screens reveal a human stem cell dependence on mRNA translation-coupled quality control

Rodschinka, G., Forcelloni, S., Kühner, F. M., Wani, S., Riemenschneider, H., Edbauer, D., Behrens, A., & Nedialkova, D. D. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01616-3 · Cited by 4

An inhibitor of GCN2 and the integrated stress response directly targets ZAK protein kinase to limit cytotoxicity

Misra, J., Spandau, D. F., Vilseck, J. Z., Anthony, T. G., Staschke, K. A., & Wek, R. C. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.111482 · Cited by 4

Druggable genome-wide Mendelian randomization for identifying the role of integrated stress response in therapeutic targets of bipolar disorder

Zhai, T. (2024) · Journal of Affective Disorders · doi:10.1016/j.jad.2024.07.043 · Cited by 5

Idiopathic Pulmonary Fibrosis Caused by Damaged Mitochondria and Imbalanced Protein Homeostasis in Alveolar Epithelial Type II Cell

Dong, Z., Wang, X., Wang, P., Bai, M., Wang, T., Chu, Y., & Qin, Y. (2024) · Advanced Biology · doi:10.1002/adbi.202400297 · Cited by 6

Reciprocal Dynamics of Metabolism and mRNA Translation in Tumor Angiogenesis

Lidonnici, J., & Oberkersch, R. E. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252011284 · Cited by 4

Role of Mitochondrial Unfolding Protein Response in Reproduction and Aging with Utilization of Autologous Mitochondrial Injections in Mitochondrial Diseases along with in Aging Oocytes

Kaur, K. K. (2020) · Open Access Journal of Gynecology · doi:10.23880/oajg-16000187 · Cited by 3

Curating gene sets: challenges and opportunities for integrative analysis

Bubier, J. A., Hill, D. P., Mukherjee, G., Reynolds, T., Baker, E. J., Berger, A., Emerson, J., Blake, J. A., & Chesler, E. J. (2019) · Database · doi:10.1093/database/baz036 · Cited by 4

Molecular basis of neurodegeneration in a mouse model of Polr3-related diseasePreprint

Moir, R. D., Merheb, E., Chiţu, V., Stanley, E. R., & Willis, I. M. (2024) · eLife · doi:10.7554/elife.95314 · Cited by 4

The Osgin Gene Family: Underexplored Yet Essential Mediators of Oxidative Stress

Hussey, G., Royster, M. O., Vaidy, N., Culkin, M., & Saha, M. S. (2025) · Biomolecules · doi:10.3390/biom15030409 · Cited by 4

Lysyl-tRNA synthetase orchestrates translation and hormone signaling during reproduction in Aedes aegypti mosquitoes

Li, S. E., Wang, X., Lu, H., Raikhel, A. S., & Zou, Z. (2025) · Communications Biology · doi:10.1038/s42003-025-08428-7 · Cited by 3

GIGYF2: A Multifunctional Regulator at the Crossroads of Gene Expression, mRNA Surveillance, and Human Disease

Zhao, C.-S., Liu, S., Li, Z., Chen, J.-Y., & Xiong, X. (2025) · Cells · doi:10.3390/cells14131032 · Cited by 3

Differential cell survival outcomes in response to diverse amino acid stress

Russier, M., Fiore, A., Bici, A., Groß, A., Tanzer, M. C., Yeroslaviz, A., Mann, M., & Murray, P. J. (2025) · Life Science Alliance · doi:10.26508/lsa.202503324 · Cited by 3

PERK protein kinase facilitates keratinocyte collective cell migration by engagement with cell adhesion molecules, independent of its kinase activity

Diaz, M. B., Staschke, K. A., Baucum, A. J., Spandau, D. F., & Wek, R. C. (2025) · Molecular Biology of the Cell · doi:10.1091/mbc.e25-06-0277 · Cited by 3

The promiscuous ribosomal P-stalk: a new functional portrait

Tchórzewski, M., & Michalec‐Wawiórka, B. (2025) · Trends in Cell Biology · doi:10.1016/j.tcb.2025.09.003 · Cited by 3

The regulation, function and disease relevance of cytoplasmic tRNAs

Stanley, R. E., Lowe, T. M., & Ignatova, Z. (2026) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-026-00963-3 · Cited by 5

GCN2 drives diurnal patterns in the hepatic integrated stress response and maintains circadian rhythms in whole body metabolism during amino acid insufficiency

Levy, J. L., Mirek, E. T., Rodriguez, E. M., Tolentino, M. J., Zalma, B. A., Roepke, T. A., Wek, R. C., Cao, R., & Anthony, T. G. (2024) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00129.2024 · Cited by 3

Translational control by general control nonderepressible 2 kinase regulates methylglyoxal-induced pain in mice

Meyer, A. R., García, G., Mikesell, A. R., O'Flanagan, S., Stucky, C. L., & Campbell, Z. T. (2025) · Pain · doi:10.1097/j.pain.0000000000003761 · Cited by 4

An Integrated Approach to Studying Rare Neuromuscular Diseases Using Animal and Human Cell-Based Models

Hines, T. J., Lutz, C. M., Murray, S. A., & Burgess, R. W. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.801819 · Cited by 4

The amino-acid stress sensing eIF2α kinase GCN2 is a survival biomarker for malignant mesothelioma

Gold, L. T., Bray, S. E., Kernohan, N. M., Henderson, N., Nowicki, M., & Masson, G. R. (2023) · BJC Reports · doi:10.1038/s44276-023-00004-y · Cited by 3

Norovirus infection results in assembly of virus-specific G3BP1 granules and evasion of eIF2α signalingPreprint

Brocard, M., Iadevaia, V., Klein, P., Hall, B. S., Lewis, G., Lu, J. Q., Burke, J. M., Parker, R., Ruggieri, A., Goodfellow, I., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/490318 · Cited by 3

RNA triggers chronic stress during neuronal agingPreprint

Rhine, K., Epstein, E., Carlson, N. M., Ge, X., Mizrahi, O., Kamat, A., Hermann, A., Brothers, W. R., Ravits, J., Bennett, E. J., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.04.668575 · Cited by 3

tRNA synthetase activity is required for stress granule and P-body assemblyPreprint

Baymiller, M., Helton, N. S., Dodd, B. J. T., & Moon, S. L. (2026) · Genes & Development · doi:10.1101/gad.353535.125 · Cited by 5

The integrated stress response: From basic mechanisms to a unified approach to treating cognitive disorders of different etiologies

Liu, Y., Boone, M., Walter, P., & Costa‐Mattioli, M. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-15754-7.00085-7 · Cited by 2

Allosteric disordering of eIF2B regulates the integrated stress response

Dalwadi, U., Subramanian, A., Deal, A., Conrad, J. E., Nadjsombati, T., Venkatesh, M., Boone, M., Egea, P. F., He, L.-J., Jain, N., et al. (2026) · Nature Chemical Biology · doi:10.1038/s41589-026-02256-4 · Cited by 2

Loss of O-GlcNAcylation in cardiac myocytes triggers the integrated stress response, contributing to heart failure

Papanicolaou, K. N., Zhang, W., Dunphy, A. J., Zhong, J. C., Cho, C., Turner, D. R., Ashok, D., Foster, D. B., O'Rourke, B. P., & Zachara, N. E. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110818 · Cited by 2

Is bRaQCing bad? New roles for ribosome associated quality control factors in stress granule regulation

Helton, N. S., & Moon, S. L. (2022) · Biochemical Society Transactions · doi:10.1042/bst20220549 · Cited by 2

Circadian clock control of interactions between eIF2α kinase CPC-3 and GCN1 with ribosomes regulates rhythmic translation initiation

Preh, E. O., Ramirez, M. A., Mohan, S., Guy, C. R., & Bell‐Pedersen, D. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2411916122 · Cited by 2

Purification and Analysis of eIF2α Phosphorylation by Stress-Activated Protein Kinase Gcn2 from S. cerevisiae

Gupta, R., Gaikwad, S., Qui, H., Bou‐Nader, C., Zhang, J., & Hinnebusch, A. G. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-4284-9_10 · Cited by 2

Nonequivalence of Zfp423 premature termination codons in mice

Concepcion, D., Liang, C., Kim, D., & Hamilton, B. A. (2025) · GENETICS · doi:10.1093/genetics/iyaf164 · Cited by 1

Amino acid restriction sensitizes lung cancer cells to ferroptosis via GCN2-dependent activation of the integrated stress response

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The ribosomal landscape in influenza A virus infection: from molecular mechanisms to clinical relevance

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CRISPuRe-seq: pooled screening of barcoded ribonucleoprotein reporters reveals regulation of RNA polymerase III transcription by the integrated stress response via mTOR

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METTL2 forms a complex with the DALRD3 anticodon-domain binding protein to catalyze formation of 3-methylcytosine in specific arginine tRNA isoacceptorsPreprint

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Serine mistranslation induces the integrated stress response without accumulation of uncharged tRNAsPreprint

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Molecular basis of neurodegeneration in a mouse model of Polr3-related diseasePreprint

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Parallel networks that govern the transcriptional response to stress

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Gcn1 inhibits initiation of ribosome-associated quality controlPreprint

Chan, T. Y. K., Choo, W. Y. X., Yoon, M.-J., & Choe, Y. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.05.04.722640 · Cited by 1

RNF25 is activated as a response to amino acid starvation-induced ribosome collisions in competition with GCN2Preprint

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最小のオープンリーディングフレームである「AUG-stop」を介した新規な遺伝子発現制御機構の発見

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Chemical Damage to mRNA and Its Impact on Ribosome Quality-Control and Stress-Response Pathways in Eukaryotic Cells

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Ribosome changes elicit non-canonical translation for chemosurvival in G0 leukemic cellsPreprint

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Faculty Opinions recommendation of The ribosomal P-stalk couples amino acid starvation to GCN2 activation in mammalian cells.

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Faculty Opinions recommendation of Translational Control through Differential Ribosome Pausing during Amino Acid Limitation in Mammalian Cells.

Bazzini, A., & Wu, Q. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733671641.793549014

Translation feedback control in the brain

Moon, S. L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00741-z

Molecular basis of neurodegeneration in a mouse model of Polr3-related diseasePreprint

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Structural Impact of 3-Methylcytosine Modification on the Anticodon Stem of a Neuronally-Enriched Arginine TrnaPreprint

Berger, K. D., Puthenpeedikakkal, A. M. K., Mathews, D. H., & Fu, D. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.18.624017

The cytosolic cysteinyl-tRNA synthetase is capable of regulating ATF4 translation independent of eIF2α phosphorylation statePreprint

Xu, A. E., & Weissman, J. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.12.23.630120

GTPBP1 resolves paused ribosomes to maintain neuronal homeostasis

Terrey, M., Adamson, S. I., Gibson, A. L., Deng, T. Z., Ishimura, R., Chuang, J. H., & Ackerman, S. L. (2020) · eLife · doi:10.7554/elife.62731 · Cited by 46

Activation of GCN2 by the ribosomal P-stalk

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The ribosomal P-stalk couples amino acid starvation to GCN2 activation in mammalian cells

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Insights into the role of collided ribosomes during the activation of the integrated stress response

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Translation feedback control in the brain

Moon, S. L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00741-z